ID A0A059B806_EUCGR Unreviewed; 864 AA.
AC A0A059B806;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=EUGRSUZ_H04495 {ECO:0000313|EMBL:KCW61795.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW61795.1};
RN [1] {ECO:0000313|EMBL:KCW61795.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW61795.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plant lipoxygenase may be involved in a number of diverse
CC aspects of plant physiology including growth and development, pest
CC resistance, and senescence or responses to wounding.
CC {ECO:0000256|RuleBase:RU003975}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962,
CC ECO:0000256|RuleBase:RU003974};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC {ECO:0000256|RuleBase:RU003975}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family.
CC {ECO:0000256|ARBA:ARBA00009419, ECO:0000256|RuleBase:RU003974}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR EMBL; KK198760; KCW61795.1; -; Genomic_DNA.
DR RefSeq; XP_010025196.1; XM_010026894.2.
DR AlphaFoldDB; A0A059B806; -.
DR STRING; 71139.A0A059B806; -.
DR EnsemblPlants; KCW61795; KCW61795; EUGRSUZ_H04495.
DR GeneID; 104415564; -.
DR Gramene; KCW61795; KCW61795; EUGRSUZ_H04495.
DR KEGG; egr:104415564; -.
DR eggNOG; ENOG502QVKD; Eukaryota.
DR InParanoid; A0A059B806; -.
DR OMA; FDSTPDE; -.
DR OrthoDB; 462210at2759; -.
DR UniPathway; UPA00382; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01751; PLAT_LH2; 1.
DR Gene3D; 3.10.450.60; -; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001246; LipOase_plant.
DR InterPro; IPR042057; Lipoxy_PLAT/LH2.
DR InterPro; IPR027433; Lipoxygenase_dom_3.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771:SF126; LINOLEATE 9S-LIPOXYGENASE 1; 1.
DR PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00468; PLTLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR SUPFAM; SSF48484; Lipoxigenase; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|RuleBase:RU003975};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003974};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU003975};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003974};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003974};
KW Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767,
KW ECO:0000256|RuleBase:RU003975}.
FT DOMAIN 39..164
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 167..864
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 218..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 864 AA; 97969 MW; 71A25EC48013486A CRC64;
MDKVIRGIRH AFDGGNEAGG SKKVKGTVVL MKKNVLDFND FNASVLDRVH ELFGQKISLQ
LVSAVHGDPE KGLRGKLGKP AYLEDWITTI TPLTAGDSAF KVTFDWDEEV GVPGAIIVQN
KHHSQFYLKT VTLEDVPGEG QVHFVCNSWV YPADQYKKER VFFSNKTYLP GQTPAPLVKY
REEELVNLRG DGTGELQEWD RVYDYAYYND LGNPDKDPKY ARPVLGGSAE YPYPRRGRTG
RPPTKTDPNT ESRVPVLMSL DIYVPRDERF GHLKMSDFLA YALKAVAQLL KPELESLYDS
TPTEFDSFKD VLKLYEGGIK LPSPLLESLE ESIPLEMIKE LVRTDGEGLL EYPIPQVIKE
NETAWRTDVE FGREMLAGVN PVLIRRLEEF PPASKLDPKI YGNQNSTIRE ELIQKQLNGL
TVKQAIKMNK LFILDHHDAI MPYLRRINTT NTKTYATRTL LFLKDDGTLK PLAIELSLPH
PEGDKFGAIS KVYMPADQGV EGSIWQLAKA YAAVNDSGYH QLVSHWLNTH AAIEPFVIAT
NRQLSALHPI YKLLHPHFRD TMNINAFARQ ILINAGGILE ATVFPAKYAM EMSSAVYKNW
IFPEQALPAD LIKRGVAVED ANSPHGLRLL IEDYPYAVDG LEIWSAIKTW VEDYCSFYYK
SDETVQKDEE LQSWWKELVE EGHGDKKDEP WWPKMQTVKD LTETCTITIW IASALHAAVN
FGQYPYAGYL PNRPTLSRRY MPEEGTPEFE ELRQNPDKAF LKTITAQLQT LLGISIIEIL
SMHSTDEVYL GQRDTREWTA DAEPLEAFER FGKKLGEVEE TIIRMNGDKR WRNRVGPVEI
PYMLLYPTSE GGVTAKGIPN SVSI
//
